Rapid folding of the prion protein captured by pressure-jump

Jenkins, David C. and Pearson, David S. and Harvey, Andrew and Sylvester, Ian D. and Geeves, Michael A. and Pinheiro, Teresa J. T. (2009) Rapid folding of the prion protein captured by pressure-jump. European Biophysics Journal, 38 (5). pp. 625-635. ISSN 0175-7571. (doi:https://doi.org/10.1007/s00249-009-0420-6) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1007/s00249-009-0420-6

Abstract

The conversion of the cellular form of the prion protein (PrP(C)) to an altered disease state, generally denoted as scrapie isoform (PrP(Sc)), appears to be a crucial molecular event in prion diseases. The details of this conformational transition are not fully understood, but it is perceived that they are associated with misfolding of PrP or its incapacity to maintain the native fold during its cell cycle. Here we present a tryptophan mutant of PrP (F198W), which has enhanced fluorescence sensitivity to unfolding/refolding transitions. Equilibrium folding was studied by circular dichroism and fluorescence. Pressure-jump experiments were successfully applied to reveal rapid submillisecond folding events of PrP at temperatures not accessed before.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 26 Apr 2012 14:59 UTC
Last Modified: 20 May 2014 15:42 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/29364 (The current URI for this page, for reference purposes)
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